A linker peptide with high affinity towards silica-containing materials

Anwar Sunna*, Fei Chi, Peter L. Bergquist

*Corresponding author for this work

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

A peptide sequence with affinity to silica-containing materials was fused to a truncated form of Streptococcus strain G148 Protein G. The resulting recombinant Linker-Protein G (LPG) was produced in Escherichia coli and purified to apparent homogeneity. It displayed high affinity towards two natural clinoptilolite zeolites. The LPG also displayed high binding affinity towards commercial-grade synthetic zeolite, silica and silica-containing materials. A commercial sample of the truncated Protein G and a basic protein, both without the linker, did not bind to natural or synthetic zeolites or silica. We conclude that the zeolite-binding affinity is mediated by the linker peptide sequence. As a consequence, these data may imply that the binding affinity is directed to the SiO2 component rather than to the atomic orientation on the zeolite crystal surface as previously assumed.

Original languageEnglish
Pages (from-to)485-492
Number of pages8
JournalNew Biotechnology
Volume30
Issue number5
DOIs
Publication statusPublished - 25 Jun 2013

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